Solution NMR studies of amphibian antimicrobial peptides: Linking structure to function?

Biochimica et Biophysica Acta - Biomembranes

Volumn 1788, Issue 8, 2009, Pages 1639-1655

  Haney, Evan F ^a   Hunter, Howard N ^a   Matsuzaki, Katsumi ^b   Vogel, Hans J ^a  

^a UNIVERSITY OF CALGARY   (Canada)

^b KYOTO UNIVERSITY   (Japan)

Author keywords

Amphibian antimicrobial peptide; Antimicrobial peptide synergy; Nuclear magnetic resonance; Peptide membrane interaction; Solution structure

Indexed keywords

AUREIN 1.2; AUREIN 2.2; AUREIN 2.3; BREVININ 2; BUFORIN 2; CAERIN 1.1; CAERIN 1.4; CAERIN 4.1; CAERIN DERIVATIVE; CITROPIN 1.1; DERMASEPTIN B2; DERMASEPTIN S9; ESCULENTIN 1A; FRENATIN 3; GAEGURIN 4; HYLASEPTIN P1; MACULATIN 1.1; MAGAININ 2; NIGROCIN 2; PEPTIDYLGLYCYLLEUCINE CARBOXYAMIDE; POLYPEPTIDE ANTIBIOTIC AGENT; RANACYCLIN T; RANALEXIN; RANATEURIN 2CSA; TEMPORIN A; TEMPORIN L; UNCLASSIFIED DRUG; UPERIN 3.6;

AMINO ACID SEQUENCE; ANTIMICROBIAL ACTIVITY; DRUG CONFORMATION; DRUG DESIGN; DRUG DETERMINATION; DRUG STRUCTURE; MEMBRANE BINDING; MICELLE; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; REVIEW; STRUCTURE ACTIVITY RELATION; XENOPUS LAEVIS;

AMINO ACID SEQUENCE; AMPHIBIAN PROTEINS; ANTI-INFECTIVE AGENTS; ANTIMICROBIAL CATIONIC PEPTIDES; MAGAININS; MAGNETIC RESONANCE SPECTROSCOPY; MOLECULAR SEQUENCE DATA; SOLUTIONS; STRUCTURE-ACTIVITY RELATIONSHIP;

AMPHIBIA; BACTERIA (MICROORGANISMS);

EID: 67649277613     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2009.01.002     Document Type: Review

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